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LOCUS WP_000689844 232 aa linear BCT 03-JUN-2024 nucleosidase [Enterobacteriaceae]. ACCESSION WP_000689844 VERSION WP_000689844.1 KEYWORDS RefSeq. SOURCE Enterobacteriaceae ORGANISM Enterobacteriaceae Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales. REFERENCE 1 (residues 1 to 232) AUTHORS Sekowska,A. and Danchin,A. TITLE The methionine salvage pathway in Bacillus subtilis JOURNAL BMC Microbiol 2, 8 (2002) PUBMED 12022921 REMARK Publication Status: Online-Only REFERENCE 2 (residues 1 to 232) AUTHORS Lee,J.E., Cornell,K.A., Riscoe,M.K. and Howell,P.L. TITLE Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases JOURNAL Structure 9 (10), 941-953 (2001) PUBMED 11591349 REFERENCE 3 (residues 1 to 232) AUTHORS Sekowska,A. and Danchin,A. TITLE Identification of yrrU as the methylthioadenosine nucleosidase gene in Bacillus subtilis JOURNAL DNA Res 6 (5), 255-264 (1999) PUBMED 10574451 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: TIGR01704.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..232 /organism="Enterobacteriaceae" /db_xref="taxon:543" gene 1..232 /gene="mtnN" Protein 1..232 /product="5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase" /EC_number="3.2.2.16" /EC_number="3.2.2.9" /GO_function="GO:0008782 - adenosylhomocysteine nucleosidase activity [Evidence IEA]" /GO_function="GO:0008930 - methylthioadenosine nucleosidase activity [Evidence IEA]" /GO_process="GO:0009164 - nucleoside catabolic process [Evidence IEA]" /GO_process="GO:0019509 - L-methionine salvage from methylthioadenosine [Evidence IEA]" /calculated_mol_wt=24223 Region 1..230 /region_name="PRK05584" /note="5'-methylthioadenosine/adenosylhomocysteine nucleosidase" /db_xref="CDD:180148" Site order(8..9,12,50..51,76..78,150..151,171..174,193, 196..197,199,212) /site_type="active" /db_xref="CDD:350159" Site order(10,31,47,49..54,56..57,60..61,63..65,97,99,149..151, 173,177,180..181,183..186) /site_type="other" /note="homodimer interface [polypeptide binding]" /db_xref="CDD:350159" ORIGIN 1 mkigiigame eevtllrdki enrqtislgg ceiytgqlng tevallksgi gkvaaalgat 61 lllehckpdv iintgsaggl aptlkvgdiv vsdearyhda dvtafgyeyg qlpgcpagfk 121 addkliaaae aciaelnlna vrglivsgda fingsvglak irhnfpqaia vemeataiah 181 vchnfnvpfv vvraisdvad qqshlsfdef lavaakqssl mveslvqkla hg